The field of this invention is growth factors, particularly fibroblast growth factors.
Basic fibroblast growth factors (bFGF)(also known as FGF2), so named because they contain a high number of basic amino acid residues (lysine, arginine and histidine) and therefore are cations at neutral pH, are potent mitogens for vascular endothelial cells in vitro and stimulate new capillary growth in vivo, i.e. they are angiogenic. Both human and bovine forms of basic FGF have been isolated, and the genes expressing these products have been cloned and sequenced. In addition, bFGF has been found to be expressed in a wide variety of tissue types, including pituitary, brain, adrenal gland, corpus luteum, retina, kidney, placenta, etc.
Patents of interest describing basic fibroblast growth factors include: U.S. Pat. Nos. 5,639,868; 5,604,293; 5,514,652; 5,478,740; 5,464,774; 5,459,015; 5,439,818; 5,352,589; 5,348,863; 5,331,095; 5,155,214; 5,143,829; 5,136,025; 5,130,418; 5,026,839; 4,994,559; 4,956,455.
Other References of interest include: Iwane et al, xe2x80x9cExpression of cDNA Encoding Human Basic Fibroblast Growth Factor in E. coli,xe2x80x9d Biochem. Biophys. Res. Comm. (1987)146:470-477; Thompson et al, xe2x80x9cCloning, Recombinant Expression, and Characterization of Basic Fibroblast Growth Factor,xe2x80x9d Methods Enzymol. (1991)198:96-116; Fox et al, xe2x80x9cProduction, Biological Activity, and Structure of Recombinant Basic Fibroblast Growth Factor and an Analog . . . ,xe2x80x9d J. Biol. Chem. (1988) 263:18452-18458; Thompson et al, xe2x80x9cThe Disulfide Structure of Bovine Pituitary Basic Fibroblast Growth Factor,xe2x80x9d J. Biol. Chem. (1992) 267:2269-2273; Conn et al, xe2x80x9cThe Isolation and Purification of Two Anionic Endothelial Cell Growth Factors from Human Brain,xe2x80x9d Biochem. Biophys. Res. Comm.(1984) 124:262-268; Bohlen et al., xe2x80x9cAcidic Fibroblast Growth Factor (FGF) from Bovine Brain: Amino-Terminal Sequence and Comparison with Basic FGF,xe2x80x9d EMBO J. (1985) 4:1951-1956; Abraham et al., J. Cell. Biochem. (1987) Supplement, vol. 0, No. 11, p. 50, Abst No. 191; Guillermo Gimenez-Gallego et al., Biochem. Biophy. Res. Communications (1986)135: 541-548; Esch et al. Proc. Natl. Acad. Sci. USA, (1985) 82: 6507-6511; Bohlen et al., Proc. Natl. Acad. Sci., USA, (1984) 81: 5364-5368; Gospodarowicz et al., Biochem. Biophy. Res. Communications (1985) 128: 554-562.
Peptidic compositions capable of binding to the FGF receptor, as well as fusion proteins and oligomers of the same, are provided. The subject peptidic compositions are characterized by having substantially no sequence homology to known naturally occurring FGF receptor ligands and may further exhibit one or more FGF activities. The subject fusion proteins comprise the peptidic composition joined to an oligomerization (e.g. dimerization) domain, either directly or through a linker group and optionally further include a heparin binding domain. The subject compositions find use in a variety of applications, including diagnostic and therapeutic applications.